ID   THRC_BUCAP              Reviewed;         429 AA.
AC   Q8K9V1;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   27-MAR-2024, entry version 109.
DE   RecName: Full=Threonine synthase;
DE            Short=TS;
DE            EC=4.2.3.1;
GN   Name=thrC; OrderedLocusNames=BUsg_186;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
CC   -!- FUNCTION: Catalyzes the gamma-elimination of phosphate from L-
CC       phosphohomoserine and the beta-addition of water to produce L-
CC       threonine. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-homoserine = L-threonine + phosphate;
CC         Xref=Rhea:RHEA:10840, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57590, ChEBI:CHEBI:57926; EC=4.2.3.1;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC       from L-aspartate: step 5/5.
CC   -!- SIMILARITY: Belongs to the threonine synthase family. {ECO:0000305}.
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DR   EMBL; AE013218; AAM67751.1; -; Genomic_DNA.
DR   RefSeq; WP_011053718.1; NC_004061.1.
DR   AlphaFoldDB; Q8K9V1; -.
DR   SMR; Q8K9V1; -.
DR   STRING; 198804.BUsg_186; -.
DR   GeneID; 75258937; -.
DR   KEGG; bas:BUsg_186; -.
DR   eggNOG; COG0498; Bacteria.
DR   HOGENOM; CLU_015170_0_0_6; -.
DR   UniPathway; UPA00050; UER00065.
DR   Proteomes; UP000000416; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0004795; F:threonine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   Gene3D; 3.90.1380.10; Threonine synthase, N-terminal domain; 1.
DR   InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR   InterPro; IPR029144; Thr_synth_N.
DR   InterPro; IPR037158; Thr_synth_N_sf.
DR   InterPro; IPR004450; Thr_synthase-like.
DR   InterPro; IPR001926; TrpB-like_PALP.
DR   InterPro; IPR036052; TrpB-like_PALP_sf.
DR   NCBIfam; TIGR00260; thrC; 1.
DR   PANTHER; PTHR42690; THREONINE SYNTHASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR42690:SF1; THREONINE SYNTHASE-LIKE 2; 1.
DR   Pfam; PF00291; PALP; 1.
DR   Pfam; PF14821; Thr_synth_N; 1.
DR   SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR   PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Lyase; Pyridoxal phosphate;
KW   Threonine biosynthesis.
FT   CHAIN           1..429
FT                   /note="Threonine synthase"
FT                   /id="PRO_0000185628"
FT   MOD_RES         108
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   429 AA;  48585 MW;  36AAB233D3C47BE6 CRC64;
     MKLYNLKNHN EQVNFETAVK LGLGQKQGLF FPVKLPIMTP VELSKILKMD FITRSTEILS
     KFISSEISKE VLHEHVKKAF SFSKPLKICI NKNISCFELF HGPTLAFKDF GARFMAQMIL
     CLNKKNESFT ILTATSGDTG AAVAHAFYGM KNIRVIILYP KGKITLLQEQ LFCTLGKNIK
     TISINGSFDD CQKLVKKAFD DKKLKESIGL NSANSINISR LLAQICYYFE AFSLISEEKR
     KNLVIAVPCG NFGNLTAGLL AKSLGLPIQS FIACTNSNDT VPRFLNSGKW NPKKTVSTIS
     NAMDISCPNN WPRIEELFRR KKWDLKELRF GSVSDNVTKE TLKELFRMGY VSEPHAAIAY
     RLLHDQLKKE EFGLFLGTAH PSKFKDTVEK ILENSISLPK ELKNRNNLPL LSHNINPDFN
     KLKEFLLEK
//